1Z5B
Topoisomerase VI-B, ADP AlF4- bound dimer form
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003676 | molecular_function | nucleic acid binding |
A | 0003677 | molecular_function | DNA binding |
A | 0003918 | molecular_function | DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity |
A | 0005524 | molecular_function | ATP binding |
A | 0006265 | biological_process | DNA topological change |
B | 0003676 | molecular_function | nucleic acid binding |
B | 0003677 | molecular_function | DNA binding |
B | 0003918 | molecular_function | DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity |
B | 0005524 | molecular_function | ATP binding |
B | 0006265 | biological_process | DNA topological change |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 2001 |
Chain | Residue |
A | ASN42 |
A | ADP1001 |
A | ALF3001 |
A | HOH4038 |
A | HOH4136 |
site_id | AC2 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE ALF A 3001 |
Chain | Residue |
A | GLY109 |
A | LEU110 |
A | GLY111 |
A | LYS427 |
A | ADP1001 |
A | MG2001 |
A | HOH4002 |
A | HOH4038 |
A | HOH4136 |
A | HOH4137 |
A | GLU38 |
A | GLY106 |
A | MET107 |
A | TYR108 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 2002 |
Chain | Residue |
B | ASN42 |
B | ADP1002 |
B | ALF3002 |
B | HOH3008 |
B | HOH3165 |
site_id | AC4 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE ALF B 3002 |
Chain | Residue |
B | GLU38 |
B | GLY106 |
B | MET107 |
B | TYR108 |
B | GLY109 |
B | LEU110 |
B | GLY111 |
B | LYS427 |
B | ADP1002 |
B | MG2002 |
B | HOH3003 |
B | HOH3008 |
B | HOH3089 |
B | HOH3165 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 A 4001 |
Chain | Residue |
A | GLY266 |
A | ASP267 |
A | THR268 |
A | THR269 |
A | ARG307 |
A | HOH4005 |
B | ARG307 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG B 2003 |
Chain | Residue |
B | ARG102 |
B | THR418 |
B | HOH3030 |
B | HOH3069 |
site_id | AC7 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE ADP A 1001 |
Chain | Residue |
A | ASN42 |
A | ALA46 |
A | ASP76 |
A | GLY80 |
A | ILE81 |
A | ALA89 |
A | TYR95 |
A | SER96 |
A | SER97 |
A | LYS98 |
A | GLY106 |
A | MET107 |
A | TYR108 |
A | GLY109 |
A | LEU110 |
A | GLY111 |
A | VAL112 |
A | LYS113 |
A | MG2001 |
A | ALF3001 |
A | HOH4004 |
A | HOH4009 |
A | HOH4011 |
A | HOH4012 |
A | HOH4136 |
B | PHE7 |
site_id | AC8 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE ADP B 1002 |
Chain | Residue |
B | HOH3016 |
B | HOH3165 |
A | PHE7 |
B | ASN42 |
B | ALA46 |
B | ASP76 |
B | GLY80 |
B | ILE81 |
B | ALA89 |
B | TYR95 |
B | SER96 |
B | SER97 |
B | LYS98 |
B | MET107 |
B | TYR108 |
B | GLY109 |
B | LEU110 |
B | GLY111 |
B | VAL112 |
B | LYS113 |
B | THR170 |
B | MG2002 |
B | ALF3002 |
B | HOH3007 |
B | HOH3008 |
B | HOH3010 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12505993, ECO:0000269|PubMed:15939019, ECO:0007744|PDB:1MX0, ECO:0007744|PDB:1Z59, ECO:0007744|PDB:1Z5A, ECO:0007744|PDB:1Z5B, ECO:0007744|PDB:1Z5C |
Chain | Residue | Details |
A | ASN42 | |
A | ASP76 | |
A | MET107 | |
B | ASN42 | |
B | ASP76 | |
B | MET107 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12505993, ECO:0000269|PubMed:15939019, ECO:0007744|PDB:1MX0, ECO:0007744|PDB:1Z5A, ECO:0007744|PDB:1Z5B, ECO:0007744|PDB:1Z5C |
Chain | Residue | Details |
A | SER96 | |
B | SER96 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12505993, ECO:0007744|PDB:1MX0 |
Chain | Residue | Details |
A | LYS427 | |
B | LYS427 |